Proteins Flashcards

(77 cards)

1
Q

What are the four main elements found in all proteins?

A

nitrogen

carbon

hydrogen

oxygen

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2
Q

Some proteins are involved in gene expression and include ___ which assists in synthesizing RNA from DNA. Other proteins are considered defensive proteins and include ___which help destroy microorganisms.

A

RNA Polymerase, antibodies

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3
Q

Proteins are made up of chains of ___ acids.

A

amino

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4
Q

What are the three major structural components of an amino acid?

A

Side chain (R)

Carboxyl group

Amino group

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5
Q

An amino acid may be described as nonpolar, polar uncharged, or polar charged based on the chemical properties of its ___ chain.

A

side (R)

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6
Q

The main elements that make up proteins are carbon, hydrogen, __, and __, in addition to small amounts of other elements, like sulfur.

A

nitrogen, oxygen

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7
Q

How do the amino acid side chains affect proteins?

A

Amino acid side chains play a critical role in the structure and function of a protein.

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8
Q

Cell signaling protein function

A

Allows cells to communicate with each other

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9
Q

Metabolic enzyme function

A

Increases the rate of a chemical reaction

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10
Q

Transporter function

A

Aids in the movement of solutes across the plasma membrane

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11
Q

Motor protein function

A

Initiates movement

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12
Q

What are the monomers found in proteins?

A

Amino acids

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13
Q

Which of the following accurately describes the chemical structure of a typical amino acid found in a protein?

  • A central carbon is bound to a carbonyl group, an amino group, and two R groups.
  • A central carbon atom is bound to an amino group, carboxyl group, a side chain, and a hydrogen atom.
  • A central carbon is double bonded to both an amino group and a carboxyl group.
A

A central carbon atom is bound to an amino group, carboxyl group, a side chain, and a hydrogen atom.

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14
Q

Amino acids are categorized based on:

A

their side chains

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15
Q

How can amino acid side chains affect the structure and function of a protein?

A

Amino acid side chains play a role in protein folding.

Amino acid side chains are involved in catalysis at the active site of enzymes.

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16
Q

What process is responsible for linking amino acids together to form polypeptides?

A

Dehydration reactions

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17
Q

In a peptide bond, which parts of the two amino acids are joined together?

A

The amino group of one amino acid and the carboxyl group of the other

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18
Q

When amino acids are linked together they form a large molecule called a(n)

A

polypeptide.

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19
Q

Proteins are made by __ reactions, in which water is removed as amino acids are linked together to form polypeptides.

A

dehydration

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20
Q

When a peptide bond is formed, two amino acids are linked between the __ group of one amino acid and the __ group of the other.

A

amino, carboxyl

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21
Q

A type of covalent bond called a ___ bond forms between the carboxyl group of one amino acid and the amino group of another amino acid.

A

peptide

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22
Q

A polypeptide is a chain of

A

amino acids

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23
Q

Between what two atoms are peptide bonds located in the backbone of a polypeptide?

A

Carbon and nitrogen

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24
Q

A free __ group is found at the N-terminus of a protein, and a free __ group is found at the C-terminus.

A

amino, carboxyl

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25
A protein whose highest level of structure is tertiary structure contains:
one polypeptide folded into its three-dimensional structure
26
Where are the peptide bonds in a polypeptide located?
In the polypeptide backbone
27
What functional groups are found at the N-terminus and the C-terminus of a polypeptide?
A carboxyl group is at the C-terminus. An amino group is at the N-terminus.
28
What is the primary structure of a protein?
The amino acid sequence of a polypeptide
29
What is the secondary structure of a protein?
The repeating pattern of folding between regions
30
Match the level of protein organization with the proper description: primary
the linear sequence of amino acids
31
Match the level of protein organization with the proper description: secondary
repetitive folding patterns such as α helix and β pleated sheet
32
Match the level of protein organization with the proper description: tertiary
the three-dimensional structure of a polypeptide
33
Match the level of protein organization with the proper description: quaternary
two or more interacting polypeptides
34
What are the two types of secondary structure found in proteins?
β pleated sheet α helix
35
Between what two atoms are peptide bonds located in the backbone of a polypeptide?
Carbon and nitrogen
36
What type of bond is responsible for the formation of α helices and β pleated sheets?
Hydrogen bond
37
The amino acid sequence of a polypeptide is called the ___ structure.
primary
38
The ___ structure of a polypeptide is the repeating pattern of folding stabilized by hydrogen bonds.
secondary
39
What level of protein organization refers to the three-dimensional shape of a polypeptide that includes all secondary structures and interactions between side chains?
Tertiary structure
40
A protein whose highest level of structure is tertiary structure contains:
one polypeptide folded into its three-dimensional structure
41
What level of protein structure is stabilized by interactions among the side chains of the polypeptide?
Tertiary structure
42
The two basic types of secondary structure are the alpha __ and the beta-pleated __.
helix, sheet
43
Proteins that have quaternary structure consist of at least __ polypeptide(s).
2
44
The elements of a polypeptide's secondary structure, the α helix and β pleated sheets are stabilized by ___ bonds.
hydrogen
45
What factors contribute to protein-protein interactions?
van der Waals effects hydrogen bonding hydrophobic effects ionic bonding
46
Match each bond or interaction with the correct description. hydrogen bond
Bond between partial positive and negative charges on different amino acids
47
Match each bond or interaction with the correct description. ionic bond
Bond between oppositely charged amino acid side chains
48
Match each bond or interaction with the correct description. disulfide bond
Covalent bond between two cysteines
49
Match each bond or interaction with the correct description. hydrophobic effect
Interaction between nonpolar amino acids
50
Match each bond or interaction with the correct description. van der Waals force
Weak, temporary attraction between two atoms
51
The three-dimensional shape of a polypeptide is the ___ structure.
tertiary
52
Which levels of protein structure are stabilized by hydrogen bonds?
Secondary structure Quaternary structure Tertiary structure
53
Interactions among the side chains of amino acids help to stabilize the ___ structure of a polypeptide.
teritary
54
What level of protein structure occurs when two or more polypeptides interact with each other to form a functional protein?
Quaternary structure
55
What type of bonds can form between positively and negatively charged side chains within a polypeptide?
Ionic bonds
56
Interactions between different proteins can be stabilized by four main factors: __ bonds, ionic bonds, __ effect, and van der __ dispersion forces.
hydrogen, hydrophobic, waals
57
Which of the following bonds and interactions contribute directly to a protein's tertiary structure? - Peptide bonds - Hydrogen bonds - Disulfide bonds - Hydrophobic effect - van der Waals forces - Glycosidic bonds - Ionic bonds
Hydrogen bonds Disulfide bonds Hydrophobic effect van der Waals forces Ionic bonds
58
Hydrogen bonds can form:
within a polypeptide and between different polypeptide chains
59
What level of protein structure is stabilized by interactions among the side chains of the polypeptide?
Tertiary structure
60
__ bonds promote protein folding when they form between oppositely-charged side chains of a protein.
hydrogen
61
Amino acid side chains that are nonpolar tend to exclude water and contribute to __ effects involved in protein folding.
hydrophobic
62
What factors contribute to protein-protein interactions?
ionic bonding hydrophobic effects hydrogen bonding van der Waals effects
63
What type of bond can form between the side R groups of two cysteine amino acids to stabilize protein structure?
Disulfide bond
64
Which levels of protein structure are stabilized by hydrogen bonds?
Quaternary structure Tertiary structure Secondary structure
65
Interactions among the side chains of amino acids help to stabilize the ___ structure of a polypeptide.
tertiary
66
What functional group is involved in disulfide bridges?
Sulfhydryl
67
Hydrophobic effects play a major role in what protein structures?
quaternary structure tertiary structure
68
___ bridges can form between the side chains of two cysteine amino acids.
Disulfide
69
A disulfide bond can form between two cysteines located:
within the same polypeptide chain or in different polypeptide chains
70
When a protein is unfolded or ______, it is no longer functional.
denatured
71
The tertiary structure of a polypeptide is predominantly determined by its __ structure.
primary
72
Disulfide bridges are covalent bonds between ___ groups of cysteine side chains.
sulfhydryl
73
Amino acid side chains that are nonpolar tend to exclude water and contribute to __ effects involved in protein folding.
hydrophobic
74
A disulfide bond between two cysteines in the same polypeptide chain can help to stabilize the ______ structure of a protein.
tertiary
75
What happens when a protein is denatured?
Its three-dimensional structure is disrupted.
76
What is the main determinant of a protein's tertiary structure?
Its primary structure
77
What functional group is involved in disulfide bridges?
Sulfhydryl